Marqusee has made important contributions to our understanding of protein folding through rigorous experimental studies. She provided the first experimental observation of an obligatory and on-pathway folding intermediate of a single protein molecule, and demonstrated that this intermediate corresponds to that seen in ensemble refolding experiments.

Research Interests

Susan Marqusee's laboratory is interested in deciphering the structural and dynamic information encoded in a protein's amino-acid sequence with the ultimate goal of understanding and predicting how changes in the sequence or environment affect a protein's energy landscape and function. She uses a combination of biophysical, structural, and computational techniques to both interrogate the energy landscape and develop new methodologies. The development of a single molecule optical tweezers approach to manipulate and observe protein conformational changes in real time provided the first glimpse of the unfolding and refolding trajectory of a single protein molecule. This approach has provided evidence for the on-pathway obligatory nature of an early folding intermediate and has identified new mechanical properties of proteins. Recent work has demonstrated the existence of parallel folding pathways in a simple two-state folding protein, clarifying an apparent discrepancy between experimental and theoretical studies and demonstrating that small changes in either the environment or sequence can alter the folding trajectory. The fundamental nature of Dr. Marqusee's work has significant impact on many other areas of research, ranging from the physical chemistry of macromolecules to the design of therapeutics that prevent the aggregation of proteins which lead to common diseases such as Alzheimer's.

These pages are for the use of PNAS Editorial Board members and authors
searching for PNAS member editors. For information about the National Academy
of Sciences or its membership, please see http://www.nasonline.org.